S23A1_RAT
ID S23A1_RAT Reviewed; 604 AA.
AC Q9WTW7;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Solute carrier family 23 member 1;
DE AltName: Full=Na(+)/L-ascorbic acid transporter 1;
DE AltName: Full=Sodium-dependent vitamin C transporter 1 {ECO:0000303|PubMed:10331392};
GN Name=Slc23a1; Synonyms=Svct1 {ECO:0000303|PubMed:10331392};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=10331392; DOI=10.1038/19986;
RA Tsukaguchi H., Tokui T., Mackenzie B., Berger U.V., Chen X.-Z., Wang Y.,
RA Brubaker R.F., Hediger M.A.;
RT "A family of mammalian Na+-dependent L-ascorbic acid transporters.";
RL Nature 399:70-75(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Sodium/ascorbate cotransporter (PubMed:10331392). Mediates
CC electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for
CC each ascorbate (By similarity). {ECO:0000250|UniProtKB:Q9UHI7,
CC ECO:0000269|PubMed:10331392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(out) + 2 Na(+)(out) = L-ascorbate(in) + 2
CC Na(+)(in); Xref=Rhea:RHEA:69883, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9UHI7};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UHI7};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UHI7}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the straight segment of
CC proximal tubules in the kidney, in intestine and liver. Detected in
CC epithelial cells of the bronchiole and epididymis.
CC {ECO:0000269|PubMed:10331392}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9UHI7}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; AF080452; AAD30367.1; -; mRNA.
DR EMBL; BC078851; AAH78851.1; -; mRNA.
DR RefSeq; NP_059011.1; NM_017315.2.
DR AlphaFoldDB; Q9WTW7; -.
DR SMR; Q9WTW7; -.
DR STRING; 10116.ENSRNOP00000027048; -.
DR TCDB; 2.A.40.6.1; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR GlyGen; Q9WTW7; 2 sites.
DR iPTMnet; Q9WTW7; -.
DR PhosphoSitePlus; Q9WTW7; -.
DR PaxDb; Q9WTW7; -.
DR PRIDE; Q9WTW7; -.
DR GeneID; 50621; -.
DR KEGG; rno:50621; -.
DR UCSC; RGD:619875; rat.
DR CTD; 9963; -.
DR RGD; 619875; Slc23a1.
DR VEuPathDB; HostDB:ENSRNOG00000061695; -.
DR eggNOG; KOG1292; Eukaryota.
DR HOGENOM; CLU_017959_5_4_1; -.
DR InParanoid; Q9WTW7; -.
DR PhylomeDB; Q9WTW7; -.
DR TreeFam; TF313272; -.
DR Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR PRO; PR:Q9WTW7; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000061695; Expressed in adult mammalian kidney and 12 other tissues.
DR ExpressionAtlas; Q9WTW7; baseline and differential.
DR Genevisible; Q9WTW7; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
DR GO; GO:0043229; C:intracellular organelle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008520; F:L-ascorbate:sodium symporter activity; IDA:RGD.
DR GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0070837; P:dehydroascorbic acid transport; ISS:UniProtKB.
DR GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISS:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; ISS:UniProtKB.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR029954; SLC23A1.
DR PANTHER; PTHR11119:SF21; PTHR11119:SF21; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..604
FT /note="Solute carrier family 23 member 1"
FT /id="PRO_0000165977"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..88
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 237..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 597
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT MOD_RES 602
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 604 AA; 65263 MW; C436A68100B713FB CRC64;
MKAQEDPGSS KQHECPDSAG TSTRDQQAPL PAEPKFDMLY KIEDVPPWYL CILLGFQHYL
TCFSGTIAVP FLLAEALCVG RDQHMISQLI GTIFTCVGIT TLIQTTVGIR LPLFQASAFA
FLVPAKAILA LERWKCPPEE EIYGNWSMPL NTSHIWHPRI REVQGAIMVS SVVEVVIGLL
GLPGALLSYI GPLTVTPTVS LIGLSVFQAA GDRAGSHWGI SACSILLIVL FSQYLRNLTF
LLPVYRWGKG LTLFRIQIFK MFPIVLAIMT VWLLCYVLTL TDVLPADPTV YGFQARTDAR
GDIMAISPWI RIPYPCQWGL PTVTVAAVLG MFSATLAGII ESIGDYYACA RLAGAPPPPV
HAINRGIFTE GVCCIIAGLL GTGNGSTSSS PNIGVLGITK VGSRRVVQYG AGIMLILGAI
GKFTALFASL PDPILGGMFC TLFGMITAVG LSNLQFVDMN SSRNLFVLGF SMFFGLTLPN
YLDSNPGAIN TGVPEVDQIL TVLLTTEMFV GGCLAFILDN TVPGSPEERG LIQWKAGAHA
NSETLASLKS YDFPFGMGMV KRTTFFRYIP ICPVFRGFSK TENQPAVLED APDNTETGSV
CTKV
